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National Chung Hsing University Institutional Repository - NCHUIR > 生命科學院 > 生命科學院 > 依資料類型分類 > 期刊論文 >  Phosphorylation of focal adhesion kinase on tyrosine 194 by Met leads to its activation through relief of autoinhibition

Please use this identifier to cite or link to this item: http://nchuir.lib.nchu.edu.tw/handle/309270000/130727

標題: Phosphorylation of focal adhesion kinase on tyrosine 194 by Met leads to its activation through relief of autoinhibition
作者: Chen, T.H.;Chan, P.C.;Chen, C.L.;Chen, H.C.
陳鴻震
關鍵字: FAK;Met;RTK;FERM;autoinhibition;growth-factor;ferm domain;in-vitro;protein;identification;pp125(fak);cells;fak;association;pp60(src)
日期: 2011
Issue Date: 2012-12-07 16:06:16 (UTC+8)
關連: Oncogene, Volume 30, Issue 2, Page(s) 153-166.
摘要: Focal adhesion kinase (FAK) has a crucial role in integration of signals from integrins and growth factor receptors. In this study, we demonstrate that growth factor receptors including hepatocyte growth factor receptor Met, epidermal growth factor receptor, and platelet-derived growth factor receptor directly phosphorylate FAK on Tyr194 in the FERM domain (band 4.1 and ezrin/radixin/moesin homology domain). Upon binding to Met or phosphoinositides, FAK may undergo conformational changes, which renders Tyr194 accessible for phosphorylation. Substitution of Tyr194 with Phe significantly suppresses the activation of FAK by Met. In contrast, substitution of Tyr194 with Glu (Y194E substitution) leads to constitutive activation of FAK. The phosphorylation of FAK on Tyr194 may cause conformational changes in the FERM domain, which disrupts the intramolecular inhibitory interaction between the FERM and kinase domains of FAK. Moreover, substitution of the basic residues in the (216)KAKTLRK(222) patch in the FERM domain with Ala antagonizes the effect of the Y194E substitution on FAK activation, thus suggesting that the interactions between the phosphorylated Tyr194 and the basic resides in the (216)KAKTLRK(222) patch may allow FAK to be activated through relief of its autoinhibition. Collectively, this study provides the first example to explain how FAK is activated by receptor tyrosine kinases. Oncogene (2011) 30, 153-166; doi:10.1038/onc.2010.398; published online 30 August 2010
Relation: Oncogene
Appears in Collections:[依教師分類] 陳正倫
[依資料類型分類] 期刊論文
[依教師分類] 陳鴻震
[依教師分類] 陳鴻震

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